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MGF

/ Synthetic peptide — C-terminal E-domain of the IGF-1Ec splice variant

TIER 3 · PreclinicalN = 0 · TESTING PENDINGMW 2867.20 g·mol⁻¹

ALIAS · Mechano Growth Factor · IGF-1Ec · IGF-I Ec splice variant · MGF (24mer C-terminal Ec peptide)

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Research use onlyAny dose figures below describe what specific cited studies used, reported factually. Nothing on this page is guidance for human use.READ FIRST →

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§ A · Identity

Primary sequenceYQPPSTNKNTKSQRRKGSTFEERK (synthetic E-domain peptide)

MW · 2867.20CLASS · Synthetic peptide — C-terminal E-domain of the IGF-1Ec splice variantCATEGORY · GH-stack

Tier 3 (animal studies only). Foundational in-vitro and rodent literature on the IGF-1Ec splice variant role in muscle damage repair; no human clinical trials of synthetic MGF peptide.

§ B · Mechanism of action

MGF (mechano growth factor) refers to the 24-residue E-domain peptide encoded by the IGF-1Ec splice variant of the human IGF-1 gene. The variant is upregulated transiently in skeletal muscle following mechanical overload or damage. The synthetic 24mer is hypothesised to act independently of the IGF-1 receptor on muscle satellite cell proliferation, while mature IGF-1 (the more abundantly produced product of the IGF-1Ea variant) drives terminal differentiation.

The downstream pathway is incompletely characterised — proposed but not definitively demonstrated mechanisms include direct activation of an unidentified cell-surface receptor, intracellular nuclear localisation, and indirect amplification of IGF-1Ea signalling through autocrine loops.

§ C · Human clinical evidence

None. No published human RCT or Phase 1 data on synthetic MGF peptide. Underlying biology is well-described in rodent and in-vitro work; clinical translation has not occurred.

§ D · Primary literature

PubMed12095637Yang SY et al. — Different roles of the IGF-I Ec peptide (MGF) and mature IGF-I in myoblast proliferation and differentiation · FEBS Letters · in-vitroSynthetic E-domain peptide of IGF-IEc (MGF) increased C2C12 myoblast proliferation but blocked differentiation, while mature IGF-I had the inverse effect — foundational evidence for distinct splice-variant roles.Limitations: Single cell line, in-vitro only; no PEGylated long-acting variants tested.2002

PubMed12692175Hill M et al. — Expression and splicing of the insulin-like growth factor gene in rodent muscle is associated with muscle satellite (stem) cell activation following local tissue damage · The Journal of Physiology · rodentMechanical overload and damage in rat muscle upregulated the IGF-I Ec (MGF) splice variant transiently and selectively, supporting the hypothesis that MGF is the early activator of satellite cells.Limitations: Small-animal mRNA study; no functional outcome on muscle force or hypertrophy.2003

§ F · Safety signal

No human safety database. Class-level concern for any IGF-1-pathway agonist is theoretical oncogenicity (IGF-1 signalling is implicated in proliferation of multiple cancer cell lines), though no direct evidence of malignancy from synthetic MGF exists.

§ H · Regulatory status

Regulatory status

FDA status:: Not FDA-approved

§ I · Notable gaps and controversies

The MGF literature is concentrated in a small number of laboratories — Geoffrey Goldspink's group at UCL produced the original characterisation and most subsequent rodent and cell-culture studies. Independent replication of the splice-variant-specific functional claims (proliferation vs differentiation) is sparse outside the founding group.

PEGylated MGF (PEG-MGF) is sold by research-chemical vendors with the marketing claim of extended half-life. The pharmacokinetic claim is plausible by analogy to other PEGylated peptides but has no published comparative half-life data in any species.